The Effect of the Low-density Lipoprotein Receptor-related Protein on Amyloid Precursor Protein Processing PDF Download
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Author: Melissa Holtman Tukey
Publisher:
ISBN:
Category : Alzheimer's disease
Languages : en
Pages : 140
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Author: Melissa Holtman Tukey
Publisher:
ISBN:
Category : Alzheimer's disease
Languages : en
Pages : 140
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Book Description
Author: Amity F. Gann
Publisher:
ISBN:
Category :
Languages : en
Pages : 92
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Book Description
![The Mechanism of the Low-density Lipoprotein Receptor-related Protein (LRP) in the Production of Amyloid-[Beta] Peptide PDF](https://books.google.com/books/content/images/frontcover/MhqhDAEACAAJ?fife=w80-h100)
Author: Eunice Chungyu Chen
Publisher:
ISBN:
Category :
Languages : en
Pages : 46
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Book Description
Alzheimer's disease (AD) is the most common form of neurodegenerative disorder affecting the elderly, presenting symptoms such as memory impairment and dementia. AD is pathologically characterized by the development of extracellular senile plaques and intracellular neurofibrillary tangles (NFT). The plaques are composed of amyloid-[Beta] peptide (A[Beta]) and the NFTs are composed of a hyperphosphorylated form of the tau protein. A[Beta] is formed by sequential proteolytic processing of the amyloid precursor protein (APP) by [Beta]-, and [Gamma]-secretase. Accordingly, alterations in APP processing result in increased A[Beta] generation. The low-density lipoprotein receptor-related protein (LRP) is a large endocytic protein involved in diverse biological functions. It has been hypothesized that LRP plays a dual role in AD, playing a role in both the clearance and the production of A[Beta]. Previous studies have shown that the cytoplasmic tail alone is able to promote A[Beta] generation and promote APP processing. This study seeks to determine the area of the cytoplasmic tail responsible for pro-amyloidogenic activity and how it occurs. Our findings indicate that the last 37 amino acids of the tail, containing a dileucine motif, are sufficient. Additionally, LRP facilitates the generation of A[Beta] by trafficking APP and BACE1 to the lipid raft domains. This function of LRP may be altered due to the presence of a Kunitz protease inhibitor (KPI) domain on APP. The results of our study have therapeutic potential to reduce [Beta]-amyloid by understanding the function of LRP in the amyloidogenic processing of APP.
![Role of the Low Density Lipoprotein Receptor-related Protein in the Metabolism of the [beta]-amyloid Precursor Protein PDF](https://books.google.com/books/content/images/frontcover/6xbcNwAACAAJ?fife=w80-h100)
Author: Paula Guillermina Ulery Torréns
Publisher:
ISBN:
Category :
Languages : en
Pages : 268
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Author: Lisa A. M. Conboy
Publisher:
ISBN:
Category : Alzheimer's disease
Languages : en
Pages : 197
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Author: David Eun-Kwang Kang
Publisher:
ISBN:
Category :
Languages : en
Pages : 390
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Author: A.D. Roses
Publisher: Springer Science & Business Media
ISBN: 3642801099
Category : Medical
Languages : en
Pages : 208
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Book Description
There is now considerable genetic evidence that the type 4 allele of the apolipoprotein E gene is a major susceptibility factor associated with late-onset Alzheimer's disease, the common form of the disease defined as starting after sixty years of age. The role of apolipoprotein E in normal brain metabolism and in the pathogenesis of Alzheimer's disease are new and exciting avenues of research. This book, written by the most outstanding scientists in this new filed, is the first presentation of results concerning the implications of apolipoprotein E on the genetics, cell biology, neuropathology, biochemistry, and therapeutic management of Alzheimer's disease.
Author: Ulrike C. Müller
Publisher: Frontiers Media SA
ISBN: 2889453553
Category :
Languages : en
Pages : 295
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Book Description
The amyloid precursor protein APP plays a key role in the pathogenesis of Alzheimer’s disease (AD), as proteolytical cleavage of APP gives rise to the Aβ peptide which is deposited in the brains of Alzheimer patients. Despite this, our knowledge of the normal cell biological and physiological functions of APP and the closely related APLPs is limited. This may have hampered our understanding of AD, since evidence has accumulated that not only the production of the Aβ peptide but also the loss of APP-mediated functions may contribute to AD pathogenesis. Thus, it appears timely and highly relevant to elucidate the functions of the APP gene family from the molecular level to their role in the intact organism, i.e. in the context of nervous system development, synapse formation and adult synapse function, as well as neural homeostasis and aging. Why is our understanding of the APP functions so limited? APP and the APLPs are multifunctional proteins that undergo complex proteolytical processing. They give rise to an almost bewildering array of different fragments that may each subserve specific functions. While Aβ is aggregation prone and neurotoxic, the large secreted ectodomain APPsα - produced in the non-amyloidogenic α-secretase pathway - has been shown to be neurotrophic, neuroprotective and relevant for synaptic plasticity, learning and memory. Recently, novel APP cleavage pathways and enzymes have been discovered that have gained much attention not only with respect to AD but also regarding their role in normal brain physiology. In addition to the various cleavage products, there is also solid evidence that APP family proteins mediate important functions as transmembrane cell surface molecules, most notably in synaptic adhesion and cell surface signaling. Elucidating in more detail the molecular mechanisms underlying these divers functions thus calls for an interdisciplinary approach ranging from the structural level to the analysis in model organisms. Thus, in this research topic of Frontiers we compile reviews and original studies, covering our current knowledge of the physiological functions of this intriguing and medically important protein family.
Author: Jorg Tatzelt
Publisher:
ISBN: 9780954333522
Category : Prions
Languages : en
Pages : 80
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Book Description
A conformational transition of the cellular prion protein (PrPC) into an aberrantly folded isoform designated scrapie prion protein (PrPSc) is the hallmark of a variety of neurodegenerative disorders collectively called prion diseases. They include Creutzfeldt-Jakob disease and Gerstmann-Stäussler-Scheinker syndrome in humans, scrapie in sheep, bovine spongiform encephalopathy (BSE) in cattle and chronic wasting disease (CWD) in free-ranging deer. In contrast to the deadly properties of misfolded PrP, PrPC seems to possess a neuroprotective activity. More-over, animal models indicated that the stress-protective activity of PrPC and the neurotoxic effects of PrPSc are somehow interconnected. In this timely book, leading scientists in the field have come together to highlight the apparently incongruous activities of different PrP conformers. The articles outline current research on celluar pathways implicated in the formation and signaling of neurotoxic and physiological PrP isoforms and delineate future research direction. Topics covered include the physiologcial activity of PrPC and its possible role as a neurotrophic factor, the finding that aberrant PrP conformers can cause neurodegeneration in the absence of infectious prion propagation, the requirement of the GPI anchor of PrPC for the neurotoxic effects of scrapie prions, the pathways implicated in the formation and neurotoxic properties of cytosolically localized PrP, the impact of metal ions on the processing of PrP, and the role of autophagy in the propagation and clearance of PrPSc. The book is fully illustrated and chapters include comprehensive reference sections. Essential reading for scientists involved in prion research.
![Opposing Roles of the LDL Receptor-related Protein (LRP1) and the LDL Receptor-related Protein 1B (LRP1B) in [beta]-amyloid Precursor Protein (APP) Trafficking and Processing PDF](https://books.google.com/books/content/images/frontcover/GPIdOAAACAAJ?fife=w80-h100)
Author: Judith Ann Cam
Publisher:
ISBN:
Category :
Languages : en
Pages : 342
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Book Description
